G3PT_RAT
ID G3PT_RAT Reviewed; 432 AA.
AC Q9ESV6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific;
DE EC=1.2.1.12;
DE AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2;
DE Short=GAPDH-2;
DE AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase;
GN Name=Gapdhs; Synonyms=Gapd-s, Gapds;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Testis;
RA McLaughlin E.A., Hall L.;
RT "Nucleotide sequence of rat testis-specific glyceraldehyde-3-phosphate
RT dehydrogenase (GAPDH-2) cDNA.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 102-432 IN TETRAMER WITH E.COLI
RP GAPDH.
RX PubMed=19542219; DOI=10.1074/jbc.m109.004648;
RA Frayne J., Taylor A., Cameron G., Hadfield A.T.;
RT "Structure of insoluble rat sperm glyceraldehyde-3-phosphate dehydrogenase
RT (GAPDH) via heterotetramer formation with Escherichia coli GAPDH reveals
RT target for contraceptive design.";
RL J. Biol. Chem. 284:22703-22712(2009).
CC -!- FUNCTION: May play an important role in regulating the switch between
CC different pathways for energy production during spermiogenesis and in
CC the spermatozoon. Required for sperm motility and male fertility (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in both head and flagellum of epididymal
CC sperm. {ECO:0000269|PubMed:19423663}.
CC -!- DOMAIN: The testis-specific N-terminal extension mediates tight
CC association with the cytoskeletal fibrous sheath of the spermatozoa
CC flagellum, possibly via interchain disulfide-bonding of Cys-33 with
CC sheath components. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AJ297631; CAC05399.1; -; mRNA.
DR RefSeq; NP_076454.1; NM_023964.1.
DR PDB; 2VYN; X-ray; 2.20 A; D=102-432.
DR PDB; 2VYV; X-ray; 2.38 A; D=102-432.
DR PDBsum; 2VYN; -.
DR PDBsum; 2VYV; -.
DR AlphaFoldDB; Q9ESV6; -.
DR SMR; Q9ESV6; -.
DR STRING; 10116.ENSRNOP00000059802; -.
DR iPTMnet; Q9ESV6; -.
DR PhosphoSitePlus; Q9ESV6; -.
DR SwissPalm; Q9ESV6; -.
DR jPOST; Q9ESV6; -.
DR PaxDb; Q9ESV6; -.
DR PRIDE; Q9ESV6; -.
DR Ensembl; ENSRNOT00000028518; ENSRNOP00000028518; ENSRNOG00000021009.
DR GeneID; 66020; -.
DR KEGG; rno:66020; -.
DR UCSC; RGD:620150; rat.
DR CTD; 26330; -.
DR RGD; 620150; Gapdhs.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000160272; -.
DR HOGENOM; CLU_030140_0_1_1; -.
DR InParanoid; Q9ESV6; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q9ESV6; -.
DR TreeFam; TF300533; -.
DR BRENDA; 1.2.1.12; 5301.
DR Reactome; R-RNO-70171; Glycolysis.
DR Reactome; R-RNO-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR EvolutionaryTrace; Q9ESV6; -.
DR PRO; PR:Q9ESV6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021009; Expressed in testis and 17 other tissues.
DR ExpressionAtlas; Q9ESV6; baseline and differential.
DR Genevisible; Q9ESV6; RN.
DR GO; GO:0001669; C:acrosomal vesicle; TAS:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031514; C:motile cilium; IDA:RGD.
DR GO; GO:0035686; C:sperm fibrous sheath; ISO:RGD.
DR GO; GO:0097228; C:sperm principal piece; ISO:RGD.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISO:RGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; ISO:RGD.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Glycolysis; NAD; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..432
FT /note="Glyceraldehyde-3-phosphate dehydrogenase, testis-
FT specific"
FT /id="PRO_0000380245"
FT REGION 1..97
FT /note="Testis-specific N-terminal extension"
FT /evidence="ECO:0000250"
FT REGION 40..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 109..110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 247..249
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 307..308
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 330
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 412
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 275
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 135..143
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 205..208
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 248..264
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 266..276
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 309..316
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 323..332
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 337..347
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 351..363
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 364..369
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 379..382
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 388..392
FT /evidence="ECO:0007829|PDB:2VYN"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:2VYN"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:2VYN"
FT HELIX 414..429
FT /evidence="ECO:0007829|PDB:2VYN"
SQ SEQUENCE 432 AA; 46708 MW; EC5F08F31DC8D35C CRC64;
MSRRDVVLTN VTVVQLRRDP CPCPCPCPCP CPCPVIRPPP PPPKVEEPPP PKEEPPPPPP
PPPPPQIEPE EPKEAPPPPP PPPPPPPPPP PPPPKPAKEL TVGINGFGRI GRLVLRVCME
KGVRVVAVND PFIDPEYMVY MFKYDSTHGR YKGTVEHKNG RLVVDNLEIN VFQCKEPKEI
PWSSVGNPYV VEATGVYLSI EAASGHISSG ARRVIVTAPS PDAPMLVMGV NEKDYNPGSM
TVVSNASCTT NCLAPLAKVI HERFGIVEGL MTTVHAYTAT QKTVDGPSKK DWRGGRGAHQ
NIIPSSTGAA KAVGKVIPEL NGKLTGMAFR VPTPNVSVVD LTCRLAQPAS YTAIKEAVKA
AAKGPMAGIL AYTEDQVVST DFNGDSHSSI FDAKAGIALN DNFVKLVSWY DNEYGYSHRV
VDLLRYMFSR EK
